ID M7NRG7_PNEMU Unreviewed; 413 AA.
AC M7NRG7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
DE AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030268};
GN ORFNames=PNEG_01898 {ECO:0000313|EMBL:EMR09711.1};
OS Pneumocystis murina (strain B123) (Mouse pneumocystis pneumonia agent)
OS (Pneumocystis carinii f. sp. muris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Pneumocystomycetes; Pneumocystaceae; Pneumocystis.
OX NCBI_TaxID=1069680 {ECO:0000313|EMBL:EMR09711.1, ECO:0000313|Proteomes:UP000011958};
RN [1] {ECO:0000313|Proteomes:UP000011958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B123 {ECO:0000313|Proteomes:UP000011958};
RX PubMed=26899007; DOI=10.1038/ncomms10740;
RA Ma L., Chen Z., Huang D.W., Kutty G., Ishihara M., Wang H., Abouelleil A.,
RA Bishop L., Davey E., Deng R., Deng X., Fan L., Fantoni G., Fitzgerald M.,
RA Gogineni E., Goldberg J.M., Handley G., Hu X., Huber C., Jiao X., Jones K.,
RA Levin J.Z., Liu Y., Macdonald P., Melnikov A., Raley C., Sassi M.,
RA Sherman B.T., Song X., Sykes S., Tran B., Walsh L., Xia Y., Yang J.,
RA Young S., Zeng Q., Zheng X., Stephens R., Nusbaum C., Birren B.W.,
RA Azadi P., Lempicki R.A., Cuomo C.A., Kovacs J.A.;
RT "Genome analysis of three Pneumocystis species reveals adaptation
RT mechanisms to life exclusively in mammalian hosts.";
RL Nat. Commun. 7:10740-10740(2016).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363036}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMR09711.1}.
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DR EMBL; AFWA02000009; EMR09711.1; -; Genomic_DNA.
DR RefSeq; XP_007873872.1; XM_007875681.1.
DR AlphaFoldDB; M7NRG7; -.
DR STRING; 1069680.M7NRG7; -.
DR GeneID; 19895592; -.
DR VEuPathDB; FungiDB:PNEG_01898; -.
DR eggNOG; KOG2145; Eukaryota.
DR HOGENOM; CLU_032621_0_1_1; -.
DR OMA; SIYHRFM; -.
DR OrthoDB; 540846at2759; -.
DR Proteomes; UP000011958; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00806; TrpRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002306; Trp-tRNA-ligase.
DR NCBIfam; TIGR00233; trpS; 1.
DR PANTHER; PTHR10055:SF1; TRYPTOPHAN--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR10055; TRYPTOPHANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01039; TRNASYNTHTRP.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363036};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363036};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363036};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363036};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363036};
KW Reference proteome {ECO:0000313|Proteomes:UP000011958}.
SQ SEQUENCE 413 AA; 47458 MW; B41398A31CFA89AA CRC64;
MEDLNISCLN LKDESTIEES KDQVITPWKV EGRVVDGRTE GIDYDRLIEK FGTKYLDEAL
LERFERLIGQ KLHVFLRRGI VFSHRDFSNI LDQYEKKEPF YIYTGRGPSS SSMHLGHMVP
FLFCKWLQDV FDVPVIIQLT DDEKYLFRQE LKLEDTRRFA RENAKDIIAC GFNPEKTLIF
LDTEFVSGSF YENVVRVSKY ITYNKCKATF GFKEEDSIGK YSFVSIQAAP SFSNSFPSIF
GKRTDIPCLI PMAIDQDPYF RLTRDVADRL GYLKPSLIHT RFFPALQGHG TKMSASDENT
AIYVSDTPSQ IKNKINKHAF SGGGATLEEH RLVGGNPDID VSFTYLKYFL EDDDQLEQIR
NDYSSGKIST GELKAITINV LQKFVAEFQE RLQLVTDHTL SLFLDSNKKL KST
//
